The structure of echovirus type 12 bound to a two-domain fragment of its cellular attachment protein decay-accelerating factor (CD 55)
The structure of echovirus type 12 bound to a two-domain fragment of its cellular attachment protein decay-accelerating factor (CD 55)
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DOI：
10.1074/jbc.m311334200
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发表时间：
2004-02-27
影响因子：
4.8
通讯作者：
Lea, SM
中科院分区：
文献类型：
--
作者：
Bhella, D;Goodfellow, IG;Lea, SM
埃可病毒12型（EV12）是一种小核糖核酸病毒科的肠道病毒，使用补体调节因子衰变加速因子（CD55）作为细胞受体。我们已经计算了一个三维重建EV12结合到一个片段的ESTV组成的短共识重复结构域3和4从冷冻阴性染色电子显微镜数据（EMD代码1057）。这表明，与早期重建的结合于病毒的相关埃可病毒7型一样，附着不在病毒峡谷内，而是发生在2重对称轴附近。尽管这种一般的相似性，我们的重建揭示了受体的相互作用，这是完全不同的观察EV7。将EV11和EV11的晶体学坐标拟合到重建图中，显示受体片段的晶体结构与病毒结合受体的密度之间非常一致，从而可以明确受体相对于病毒体的位置（PDB代码1UPN）。我们的发现，在EV12的病毒受体相互作用的模式是从EV7所看到的不同，提出了有趣的问题，在这些病毒中的结合表型的进化和生物学意义。
Echovirus type 12 (EV12), an Enterovirus of the Picornaviridae family, uses the complement regulator decay-accelerating factor (DAF, CD55) as a cellular receptor. We have calculated a three-dimensional reconstruction of EV12 bound to a fragment of DAF consisting of short consensus repeat domains 3 and 4 from cryo-negative stain electron microscopy data (EMD code 1057). This shows that, as for an earlier reconstruction of the related echovirus type 7 bound to DAF, attachment is not within the viral canyon but occurs close to the 2-fold symmetry axes. Despite this general similarity our reconstruction reveals a receptor interaction that is quite different from that observed for EV7. Fitting of the crystallographic co-ordinates for DAF(34) and EV11 into the reconstruction shows a close agreement between the crystal structure of the receptor fragment and the density for the virus-bound receptor, allowing unambiguous positioning of the receptor with respect to the virion (PDB code 1UPN). Our finding that the mode of virus-receptor interaction in EV12 is distinct from that seen for EV7 raises interesting questions regarding the evolution and biological significance of the DAF binding phenotype in these viruses.